Exploring Manually Curated Annotations of Intrinsically Disordered Proteins with DisProt. Issue 7 (5th July 2022)
- Record Type:
- Journal Article
- Title:
- Exploring Manually Curated Annotations of Intrinsically Disordered Proteins with DisProt. Issue 7 (5th July 2022)
- Main Title:
- Exploring Manually Curated Annotations of Intrinsically Disordered Proteins with DisProt
- Authors:
- Quaglia, Federica
Hatos, András
Salladini, Edoardo
Piovesan, Damiano
Tosatto, Silvio C. E. - Abstract:
- Abstract: DisProt is the major repository of manually curated data for intrinsically disordered proteins collected from the literature. Although lacking a stable three‐dimensional structure under physiological conditions, intrinsically disordered proteins carry out a plethora of biological functions, some of them directly arising from their flexible nature. A growing number of scientific studies have been published during the last few decades to shed light on their unstructured state, their binding modes, and their functions. DisProt makes use of a team of expert biocurators to provide up‐to‐date annotations of intrinsically disordered proteins from the literature, making them available to the scientific community. Here we present a comprehensive description on how to use DisProt in different contexts and provide a detailed explanation of how to explore and interpret manually curated annotations of intrinsically disordered proteins. We describe how to search DisProt annotations, both using the web interface and the API for programmatic access. Finally, we explain how to visualize and interpret a DisProt entry, the SARS‐CoV‐2 Nucleoprotein, characterized by the presence of unstructured N‐terminal and C‐terminal regions and a flexible linker. © 2022 The Authors. Current Protocols published by Wiley Periodicals LLC. Basic Protocol 1 : Performing a search in DisProt Support Protocol 1 : Downloading options Support Protocol 2 : Programmatic access with DisProt REST API BasicAbstract: DisProt is the major repository of manually curated data for intrinsically disordered proteins collected from the literature. Although lacking a stable three‐dimensional structure under physiological conditions, intrinsically disordered proteins carry out a plethora of biological functions, some of them directly arising from their flexible nature. A growing number of scientific studies have been published during the last few decades to shed light on their unstructured state, their binding modes, and their functions. DisProt makes use of a team of expert biocurators to provide up‐to‐date annotations of intrinsically disordered proteins from the literature, making them available to the scientific community. Here we present a comprehensive description on how to use DisProt in different contexts and provide a detailed explanation of how to explore and interpret manually curated annotations of intrinsically disordered proteins. We describe how to search DisProt annotations, both using the web interface and the API for programmatic access. Finally, we explain how to visualize and interpret a DisProt entry, the SARS‐CoV‐2 Nucleoprotein, characterized by the presence of unstructured N‐terminal and C‐terminal regions and a flexible linker. © 2022 The Authors. Current Protocols published by Wiley Periodicals LLC. Basic Protocol 1 : Performing a search in DisProt Support Protocol 1 : Downloading options Support Protocol 2 : Programmatic access with DisProt REST API Basic Protocol 2 : Exploring the DisProt Ontology page Basic Protocol 3 : Visualizing and interpreting DisProt entries–the SARS‐CoV‐2 Nucleoprotein use case … (more)
- Is Part Of:
- Current protocols. Volume 2:Issue 7(2022)
- Journal:
- Current protocols
- Issue:
- Volume 2:Issue 7(2022)
- Issue Display:
- Volume 2, Issue 7 (2022)
- Year:
- 2022
- Volume:
- 2
- Issue:
- 7
- Issue Sort Value:
- 2022-0002-0007-0000
- Page Start:
- n/a
- Page End:
- n/a
- Publication Date:
- 2022-07-05
- Subjects:
- biocuration -- database -- DisProt -- IDPs -- intrinsically disordered proteins
Life sciences -- Laboratory manuals -- Periodicals
Biology -- Laboratory manuals -- Periodicals
Life sciences -- Technique -- Periodicals
Biology -- Technique -- Periodicals
570.028 - Journal URLs:
- https://currentprotocols.onlinelibrary.wiley.com/journal/26911299 ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1002/cpz1.484 ↗
- Languages:
- English
- ISSNs:
- 2691-1299
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 23530.xml